MolNFT v1 · #138697 · protein
Crystal structure of dodecameric type II dehydroquinate dehydratase from acinetobacter baumannii with unexplained connecting electron density between free cysteine residues of molecular pairs
5WRF: “Crystal structure of dodecameric type II dehydroquinate dehydratase from acinetobacter baumannii with…”. X-ray diffraction. MolNFT v1 #138697 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5WRF
- Type
- protein
- Length
- 1,740 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A3M692
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | — | protein | 145 | — | A3M692 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5WRF · Crystal structure of dodecameric type II dehydroquinate dehydratase from Acinetobacter… · the same entry in another collection · chain L against L, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A3M692
- Elsewhere: RCSB PDB 5WRF · PDBe 5WRF · UniProt A3M692
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.